| DOI | Resolve DOI: https://doi.org/10.1007/BF00175740 |
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| Author | Search for: Gilbert, M.; Search for: Yaguchi, M.1; Search for: Watson, D. C.1; Search for: Wong, K. K. Y.; Search for: Breuil, C.; Search for: Saddler, J. N. |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Abstract | Two thermophilic xylanases (xylanase II from Thielavia terrestris 255B and the 32-kDa xylanase from Thermoascus crustaceus 235E) were studied to determine if they had different and complementary modes of action when they hydrolysed various types of xylans. Partial amino acid sequencing showed that these two enzymes belonged to different families of β-1,4-glycanases. Xylanase II achieved faster solubilization of insoluble xylan whereas the 32-kDa xylanase was more effective in producing xylose and short xylooligomers. An assessment of the combined hydrolytic action of the two xylanases did not reveal any co-operative action. The sugars released when the two thermophilic xylanases were used together were almost identical to those released when the 32-kDa xylanase acted alone. The two xylanases were able to remove about 12% of the xylan remaining in an aspen kraft pulp. This indicated that either one of these thermophilic enzymes may be useful for enhancing the bleaching of kraft pulps. |
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| Publication date | 1993-12 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | GILBERT1993 |
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| NPARC number | 9365471 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | bd945bae-1100-4662-b1f4-688a986ebdd7 |
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| Record created | 2009-07-10 |
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| Record modified | 2020-04-24 |
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